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Auxiliary‐Mediated Site‐Specific Peptide Ubiquitylation
Author(s) -
Chatterjee Champak,
McGinty Robert K.,
Pellois JeanPhilippe,
Muir Tom W.
Publication year - 2007
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200605155
Subject(s) - ubiquitin , peptide , lysine , substrate (aquarium) , ligation , chemistry , terminal (telecommunication) , histone , photodissociation , product (mathematics) , deubiquitinating enzyme , biochemistry , computational biology , computer science , biology , microbiology and biotechnology , amino acid , mathematics , organic chemistry , telecommunications , ecology , gene , geometry
Lighting up ubiquitylation : A photolytically removable ligation auxiliary (Aux) was employed for the site‐specific attachment of ubiquitin (Ub) to one of three lysine residues in a C‐terminal peptide fragment of histone H2B (cH2B). Following photolysis, the ligation product was a viable substrate for the ubiquitin C‐terminal hydrolase UCH‐L3.